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10.1016/j.cell.2020.09.032 http://scihub22266oqcxt.onion/10.1016/j.cell.2020.09.032 32991842!7492024!32991842     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2020 ; 183 (3): 739-751.e8 Nephropedia Template TP {{tp|p=32991842|t=2020. Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant |pdf=|usr=}}{{32991842}} gab.com Text Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=32991842 #FOAvip The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin. D614G did not alter S protein synthesis, processing, or incorporation into SARS-CoV-2 particles, but D614G affinity for ACE2 was reduced due to a faster dissociation rate. Assessment of the S protein trimer by cryo-electron microscopy showed that D614G disrupts an interprotomer contact and that the conformation is shifted toward an ACE2 binding-competent state, which is modeled to be on pathway for virion membrane fusion with target cells. Consistent with this more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated. Twit Text FOAVip Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=32991842 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32991842 #FOAvip English Wikipedia <ref>{{Cite pmid|32991842}}</ref> Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant #MMPMID32991842 Yurkovetskiy L; Wang X; Pascal KE; Tomkins-Tinch C; Nyalile TP; Wang Y; Baum A; Diehl WE; Dauphin A; Carbone C; Veinotte K; Egri SB; Schaffner SF; Lemieux JE; Munro JB; Rafique A; Barve A; Sabeti PC; Kyratsous CA; Dudkina NV; Shen K; Luban J Cell 2020[Oct]; 183 (3): 739-751.e8 PMID32991842show ga The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin. D614G did not alter S protein synthesis, processing, or incorporation into SARS-CoV-2 particles, but D614G affinity for ACE2 was reduced due to a faster dissociation rate. Assessment of the S protein trimer by cryo-electron microscopy showed that D614G disrupts an interprotomer contact and that the conformation is shifted toward an ACE2 binding-competent state, which is modeled to be on pathway for virion membrane fusion with target cells. Consistent with this more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated. |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Antibodies, Monoclonal/immunology[MESH] |Antibodies, Viral/immunology[MESH] |Betacoronavirus/pathogenicity/*physiology/*ultrastructure[MESH] |COVID-19[MESH] |Cells, Cultured[MESH] |Coronavirus Infections/virology[MESH] |Female[MESH] |Genetic Variation[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Male[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/metabolism[MESH] |Pneumonia, Viral/virology[MESH] |Protein Conformation[MESH] |Protein Processing, Post-Translational[MESH] |Receptors, Coronavirus[MESH] |Receptors, Virus/metabolism[MESH] |SARS-CoV-2[MESH] |Species Specificity[MESH]Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Prote(epmc).pdf DeepDyve Pubget Overpricing